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Solubilization of 20S acetylcholinesterase from chick retina

1980; Elsevier BV; Volume: 96; Issue: 3 Linguagem: Inglês

10.1016/0006-291x(80)90109-6

1090-2104

Ana Barat, Elena Escudero, Javier Gómez‐Barriocanal, Galo Ramı́rez,

Enzyme function and inhibition

A 20S form of acetylcholinesterase has been solubilized from young chick retinas by means of a buffered salt-detergent solution containing EDTA. The release of this fast-sedimenting form of the enzyme is selectively blocked by the presence of even small amounts of Ca++ in the homogenization medium. The collagen-tailed nature of this molecular species of acetylcholinesterase has been ascertained by collagenase digestion. This finding suggests that the avian central nervous system contains asymmetric, collagen-tailed quaternary structural forms of acetylcholinesterase as is the case in skeletal muscle and cholinergic ganglia.